HBSAG_HPBDW
ID HBSAG_HPBDW Reviewed; 330 AA.
AC P17195;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Large envelope protein;
DE AltName: Full=L glycoprotein;
DE AltName: Full=L-HBsAg;
DE Short=LHB;
DE AltName: Full=Large S protein;
DE AltName: Full=Large surface protein;
DE AltName: Full=Major surface antigen;
DE Contains:
DE RecName: Full=Truncated S protein;
DE Short=St;
GN Name=S;
OS Duck hepatitis B virus (isolate white Shanghai duck S31) (DHBV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Blubervirales; Hepadnaviridae; Avihepadnavirus.
OX NCBI_TaxID=10440;
OH NCBI_TaxID=8835; Anas (ducks).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2596031; DOI=10.1016/0042-6822(89)90571-0;
RA Uchida M., Esumi M., Shikata T.;
RT "Molecular cloning and sequence analysis of duck hepatitis B virus genomes
RT of a new variant isolated from Shanghai ducks.";
RL Virology 173:600-606(1989).
CC -!- FUNCTION: The large envelope protein exists in two topological
CC conformations, one which is termed 'external' or Le-HBsAg and the other
CC 'internal' or Li-HBsAg. In its external conformation the protein
CC attaches the virus to cell receptors and thereby initiating infection.
CC This interaction determines the species specificity and liver tropism.
CC The large envelope protein probably also assumes fusion between virion
CC and host membranes. In its internal conformation the protein plays a
CC role in virion morphogenesis and mediates the contact with the
CC nucleocapsid like a matrix protein (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Truncated S protein may be involved in translocation of pre-S
CC domain through the virion membrane. {ECO:0000250}.
CC -!- SUBUNIT: Large internal envelope protein interacts with capsid protein.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=L; Synonyms=Large envelope protein, LHB, L-HBsAg;
CC IsoId=P17195-1; Sequence=Displayed;
CC Name=S; Synonyms=Small envelope protein, SHB, S-HBsAg;
CC IsoId=P17195-2; Sequence=VSP_031890;
CC -!- DOMAIN: The large envelope protein is synthesized with the pre-S region
CC at the cytosolic side of the endoplasmic reticulum and, hence will be
CC within the virion after budding. Therefore the pre-S region is not N-
CC glycosylated. Later a post-translational translocation of N-terminal
CC pre-S and TM1 domains occur in about 50% of proteins at the virion
CC surface. These molecules change their topology by an unknown mechanism,
CC resulting in exposure of pre-S region at virion surface.
CC -!- PTM: Myristoylation contributes importantly to DHBV infectivity. It is
CC most likely required for an early step of the life cycle involving the
CC entry or uncoating of virus particles.
CC -!- PTM: Phosphorylated on pre-S domain for about 50% of L proteins, the L
CC chains with internal pre-S region (Li-HBsAg).
CC -!- SIMILARITY: Belongs to the avihepadnavirus major surface antigen
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA45752.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M32991; AAA45752.1; ALT_INIT; Genomic_DNA.
DR PIR; D33746; SAVLWD.
DR Proteomes; UP000007558; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039663; P:membrane fusion involved in viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR000349; HBV_HBSAG.
DR Pfam; PF00695; vMSA; 2.
PE 3: Inferred from homology;
KW Alternative initiation; Fusion of virus membrane with host membrane;
KW Glycoprotein; Host-virus interaction; Lipoprotein; Membrane; Myristate;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral penetration into host cytoplasm;
KW Virion; Virus entry into host cell.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000250"
FT CHAIN 2..330
FT /note="Large envelope protein"
FT /id="PRO_0000038081"
FT CHAIN 164..?240
FT /note="Truncated S protein"
FT /id="PRO_0000322199"
FT TOPO_DOM 2..238
FT /note="Cytoplasmic; in internal conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2..165
FT /note="Extracellular; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical; Name=TM1; Note=In external conformation"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..238
FT /note="Cytoplasmic; in external conformation"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical; Name=TM2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..292
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical; Name=TM3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..163
FT /note="Pre-S"
FT REGION 68..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE ?240..?241
FT /note="Cleavage; by host"
FT /evidence="ECO:0000255"
FT LIPID 2
FT /note="N-myristoyl glycine; by host"
FT /evidence="ECO:0000250"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..163
FT /note="Missing (in isoform S)"
FT /evidence="ECO:0000305"
FT /id="VSP_031890"
SQ SEQUENCE 330 AA; 36787 MW; E56A456853C00775 CRC64;
MGQQPAKSMD VRRIEGGELL LNQLAGRMIP KGTVTWSGKF PTIDHLLDHV QTMEEVNTLQ
QQGAWPAGAG RRLGLTNPAP QEPPQPQWTP EEDQKAREAF RRYQEERPPE TTTIPPTSPT
PWKLQPGDDP LLENKSLLET HPLYQNPEPA VPVIKTPPLR KKKMAGTFGG ILAGLIGLLV
GFFLLIKILE ILRRLDWWWI SLSSPKGKMQ CAFQDTGAQI SPHYAGFCPW GCPGFLWTYL
RLFIIFLLIL LVAAGLLYLT DNMSIILGKL QWESVSALFS SISSLLPSDQ KSLVALMFGL
LLIWMTSSSA TQTLVTLTQL ATLSALFYKN
